Functional evidence for D- and T-loop interactions in tmRNA

During bacterial protein synthesis, stalled ribosomes can be rescued by tmRNA, a molecule with both tRNA and mRNA features. The tRNA region of tmRNA has sequence similarity with tRNA Ala and also has a clover-leaf structure folded similarly as in canonical tRNAs. Here we propose the L-shape of tmRNA...

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Bibliographic Details
Published in:FEBS letters 2002-03, Vol.514 (1), p.78-83
Main Authors: Barends, Sharief, Björk, Karl, Gultyaev, Alexander P., de Smit, Maarten H., Pleij, Cornelis W.A., Kraal, Barend
Format: Article
Language:English
Subjects:
Ala-tRNA synthetase
Alanine - metabolism
Base Sequence
Elongation factor Tu
Escherichia coli - genetics
Escherichia coli - metabolism
Molecular Sequence Data
Mutation
Nucleic Acid Conformation
Peptide Elongation Factor Tu - metabolism
RNA, Bacterial - chemistry
RNA, Bacterial - genetics
RNA, Bacterial - metabolism
RNA, Transfer, Ala - metabolism
RNA-Binding Proteins - metabolism
Sequence Homology, Nucleic Acid
SmpB
tmRNA
trans-Translation
tRNA folding
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Summary:During bacterial protein synthesis, stalled ribosomes can be rescued by tmRNA, a molecule with both tRNA and mRNA features. The tRNA region of tmRNA has sequence similarity with tRNA Ala and also has a clover-leaf structure folded similarly as in canonical tRNAs. Here we propose the L-shape of tmRNA to be stabilized by two tertiary interactions between its D- and T-loop on the basis of phylogenetic and experimental evidence. Mutational analysis clearly demonstrates a tertiary interaction between G 13 and U 342. Strikingly, this in evolution conserved interaction is not primarily important for tmRNA alanylation and for binding to elongation factor Tu, but especially for a proper functioning of SmpB.
ISSN:0014-5793
1873-3468
DOI:10.1016/S0014-5793(02)02306-2